Antidepressant drug-protein interactions studied by spectroscopic methods based on fluorescent carbon quantum dots. Issue 5 (May 2019)

• Record Type: Journal Article
• Authors: Reshma, ; Vaishanav, Sandeep K.; Yadav, Toshikee; Sinha, Srishti; Tiwari, Swapnil; Satnami, Manmohan L.; Ghosh, Kallol K.
• Is Part Of: Heliyon. Volume 5:Issue 5(2019)
• Publication Date: 2019-05
• Subjects: Physical chemistry -- Materials chemistry; Research -- Periodicals; Medical sciences -- Periodicals; Natural history -- Periodicals; Social sciences -- Periodicals; Earth sciences -- Periodicals; Physical sciences -- Periodicals; 507.2
• DOI: 10.1016/j.heliyon.2019.e01631
• Languages: English
• ISSNs: 2405-8440

Abstract

Abstract: A highly sensitive fluorescent carbon quantum dots (CDs) was designed to measure the interaction of antidepressant drugs and serum albumins (SA). In present investigation the interaction of bovine serum albumin (BSA) and human serum albumin (HSA) with antidepressant drugs viz. amitryptiline hydrochloride (AMT), chlorpromazine hydrochloride (CPZ) and desipramine hydrochloride (DSP) bioconjugated on CDs have been studied by different spectroscopic techniques i.e., Fluorescence, UV-Visible, Dynamic light scattering (DLS) and FT-IR. The CDs were prepared by one-pot method using glucose and PEG-200. The developed CDs showed blue luminescence under irradiation with ultra-violet. The Stern-Volmer quenching constant (K sv ) indicates the presence of static quenching mechanism. The apparent binding constant K a between antidepressant drugs with complex of SA-CDs have been determined. These results illustrated that CPZ shows strong binding with HSA. As further analyzed by FT-IR spectroscopy and DLS technique, the results suggested induced conformational changes on SA, thus confirming the experimental and theoretical results. Thus, a thorough knowledge of the energetics of drug-protein affinities in presence of CDs as attempted in this work is vital in giving way for appropriate drug delivery.